Abstract This study aimed to evaluate the rheological properties of pork myofibrillar protein gels (MPGs) with faba bean protein isolate (FBPI) at various salt concentrations. MPGs with 1.0% FBPI had a higher cooking yield, gel strength, protein surface hydrophobicity, and shear stress values than the control groups. The addition of FBPI resulted in more homogenous MPGs with a denser surface compared to the control groups. No interactions in rheological properties between FBPI addition and salt concentration were observed, except for gel strength. MPGs at a 0.45 M salt concentration showed a higher cooking yield and hydrophobicity and fewer sulfhydryl groups than those at a 0.15 M salt concentration. The shear stress values at a 0.45 M salt concentration dramatically increased compared to those at 0.15 M and 0.30 M. Furthermore, higher salt concentrations (0.3 M salt) resulted in fewer cavities and a more compact three-dimensional structure. Therefore, higher salt concentrations might improve the rheological properties of MPGs and influence the effects of FBPI on the viscosity and protein patterns.
Kim et al. (Thu,) studied this question.